Phosphorylation of serine‐46 in HPr, a key regulatory protein in bacteria, results in stabilization of its solution structure

Katherine Pullen; Ponni Rajagopal; Rachel E. Klevit; Bruce R. Branchini; Jonathan Reizer; Milton H. Saier; J. Martin Scholtz; Mary Elizabeth Huffine

doi:10.1002/pro.5560041204

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Phosphorylation of serine‐46 in HPr, a key regulatory protein in bacteria, results in stabilization of its solution structure

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Phosphorylation of serine‐46 in HPr, a key regulatory protein in bacteria, results in stabilization of its solution structure

Katherine Pullen, Ponni Rajagopal, Rachel E. Klevit, Bruce R. Branchini, Jonathan Reizer, Milton H. Saier, J. Martin Scholtz and Mary Elizabeth Huffine

Protein science, Vol.4(12), pp.2478-2486

12/1995

DOI: 10.1002/pro.5560041204

PMCID: PMC2143046

PMID: 8580838

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Abstract

The serine‐phosphorylated form of histidine‐containing protein (HPr), a component of the phosphoenol‐pyruvate:sugar phosphotransferase system from Bacillus subtilis, has been characterized by NMR spectroscopy and solvent denaturation studies. The results indicate that phosphorylation of Ser 46, the N‐cap of α‐helix‐B, does not cause a conformational change but rather stabilizes the helix. Amide proton exchange rates in helix‐B are decreased and phosphorylation stabilizes the protein to solvent and thermal denaturation, with a ΔΔG of 0.7‐0.8 kcal mol−1. A mutant in which Ser 46 is replaced by aspartic acid shows a similar stabilization, indicating that an electrostatic interaction between the negatively charged groups and the helix macrodipole contributes significantly to the stabilization.

NMR

protein dynamics

protein phosphorylation

protein stability

protein structure

PTS

solvent denaturation

Details

Title: Subtitle: Phosphorylation of serine‐46 in HPr, a key regulatory protein in bacteria, results in stabilization of its solution structure
Creators: Katherine Pullen - University of Washington
Ponni Rajagopal - University of Washington
Rachel E. Klevit - University of Washington
Bruce R. Branchini - Connecticut College
Jonathan Reizer - University of California San Diego
Milton H. Saier - University of California San Diego
J. Martin Scholtz - Texas A&M University
Mary Elizabeth Huffine - Texas A&M University
Resource Type: Journal article
Publication Details: Protein science, Vol.4(12), pp.2478-2486
DOI: 10.1002/pro.5560041204
PMID: 8580838
PMCID: PMC2143046
NLM abbreviation: Protein Sci
ISSN: 0961-8368
eISSN: 1469-896X
Publisher: Cold Spring Harbor Laboratory Press
Number of pages: 9
Grant note: NIH (ROl DK35187 (R.E.K.); NIH R29 GM52483 (J.M.S.); NIH 5R01 AI21702; NIH 2R01 AI14176 (M.H.S.))
Language: English
Date published: 12/1995
Academic Unit: Research Administration; Pharmaceutical Sciences and Experimental Therapeutics; Biochemistry and Molecular Biology; Chemistry
Record Identifier: 9984288725502771

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